Analytical Data
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Gene name
Try4
- Application
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Alternative Names
Try4；PRSS4；TRY3；TRY4；Trypsin-3
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Species
Rat
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P12788
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Expression Region
24-247aa
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AA Sequence
IVGGYTCPKHLVPYQVSLHDGISHQCGGSLISDQWVLSAAHCYKRKLQVRLGEHNIHVLEGGEQFIDAEKIIRHPEYNKDTLDNDIMLIKLKSPAVLNSQVSTVSLPRSCASTDAQCLVSGWGNTVSIGGKYPALLQCLEAPVLSASSCKKSYPGQITSNMFCLGFLEGGKDSCDGDSGGPVVCNGEIQGIVSWGSVCAMRGKPGVYTKVCNYLSWIQETMANN
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Molecular Weight
26.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Try4 is a protein that plays a crucial role in various biological processes, particularly in the field of microbiology and biochemistry. Research on Try4 has gained momentum due to its potential implications in understanding protein interactions, enzymatic activities, and metabolic pathways. The Try4 protein, categorized under the family of tryptophan-rich proteins, is known for its involvement in the synthesis and transport of neurotransmitters, as well as its participation in cellular stress responses. Recent studies have focused on elucidating its structure-function relationship, which could uncover novel therapeutic targets for diseases linked to neurotransmitter imbalances, such as depression and anxiety. Additionally, the exploration of Try4’s reconstitution strategies aims to facilitate its utilization in industrial applications, including biosensors and biocatalysis, leveraging its unique properties. Given the increasing interest in personalized medicine, the ability to manipulate and recombine Try4 could pave the way for innovative treatments that are tailored to individual biochemical profiles. Overall, the investigation into Try4 and its recombined forms represents an exciting frontier in the biotechnological landscape, underlining the importance of such proteins in both fundamental research and applied sciences.
